Studies are progressing on the following projects: 1. Lactose synthetase. The kinetic mechanism of the synthetase and the structure-function properties of alpha-lactalbumin and the galactosyl transferase are continuing to be examined. 2. The nature of the cross-links and the amino acid sequences around the cross-links in the alpha-chains of human fibrin are close to being elucidated. 3. Glycosyl transferases are being purified to homogeneity by affinity chromatography and their enzymatic properties established. Under study now are 2 UDP-N-acetylgalactosaminyl transferases, 3 sialyl transferases, 3 galactosyl transferases and 2-3 fucosyl transferases. The way they act in concert in the biosynthesis of oligosaccharides of glycoproteins is being established with special attention to control mechanisms. 4. The structures of ovine, porcine and bovine mucins are being elucidated including their subunit structures and partial amino acid compositions. BIBLIOGRAPHIC REFERENCES: Purification and Properties of Porcine A-Blood Group Specific N-Acetylgalactosaminyl Transferase, M. Schwyzer & R.L. Hill, (1976) Federation Proc. 35, 1441. Regulation of Glycosyl Transferases, R.L. Hill, H.D. Hill, Jr., V.R. Naik, J.C. Paulson, J.I. Rearick and M. Schwyzer. Tenth International Congress of Biochemistry, Hamburg, Germany, 1976.